NEK6_HUMAN
ID NEK6_HUMAN Reviewed; 313 AA.
AC Q9HC98; B7Z2D9; Q5TBG3; Q5TBG9; Q6FG86; Q6IAR3; Q96E83; Q9ULX2;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Serine/threonine-protein kinase Nek6;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis A-related kinase 6;
DE Short=NimA-related protein kinase 6;
DE AltName: Full=Protein kinase SID6-1512;
GN Name=NEK6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12054534; DOI=10.1016/s0006-291x(02)00297-8;
RA Hashimoto Y., Akita H., Hibino M., Kohri K., Nakanishi M.;
RT "Identification and characterization of Nek6 protein kinase, a potential
RT human homolog of NIMA histone H3 kinase.";
RL Biochem. Biophys. Res. Commun. 293:753-758(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Saito T., Saito R., Saito S.;
RT "A protein kinase weakly similar to nek1.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Kidney, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-313 (ISOFORMS 1/2/3/4).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PHOSPHORYLATION AT SER-37; THR-202 AND SER-206.
RX PubMed=12840024; DOI=10.1074/jbc.m303663200;
RA Belham C., Roig J., Caldwell J.A., Aoyama Y., Kemp B.E., Comb M.,
RA Avruch J.;
RT "A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6
RT and Nek7 kinases.";
RL J. Biol. Chem. 278:34897-34909(2003).
RN [9]
RP FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-74 AND LYS-75, AND
RP INDUCTION.
RX PubMed=14563848; DOI=10.1074/jbc.m308080200;
RA Yin M.J., Shao L., Voehringer D., Smeal T., Jallal B.;
RT "The serine/threonine kinase Nek6 is required for cell cycle progression
RT through mitosis.";
RL J. Biol. Chem. 278:52454-52460(2003).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PIN1.
RX PubMed=16476580; DOI=10.1016/j.bbrc.2005.12.228;
RA Chen J., Li L., Zhang Y., Yang H., Wei Y., Zhang L., Liu X., Yu L.;
RT "Interaction of Pin1 with Nek6 and characterization of their expression
RT correlation in Chinese hepatocellular carcinoma patients.";
RL Biochem. Biophys. Res. Commun. 341:1059-1065(2006).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH APBB1, AND PHOSPHORYLATION AT
RP THR-210.
RX PubMed=17512906; DOI=10.1016/j.bbrc.2007.04.203;
RA Lee E.J., Hyun S.H., Chun J., Kang S.S.;
RT "Human NIMA-related kinase 6 is one of the Fe65 WW domain binding
RT proteins.";
RL Biochem. Biophys. Res. Commun. 358:783-788(2007).
RN [12]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=18728393; DOI=10.4161/cc.7.17.6551;
RA Lee M.Y., Kim H.J., Kim M.A., Jee H.J., Kim A.J., Bae Y.S., Park J.I.,
RA Chung J.H., Yun J.;
RT "Nek6 is involved in G2/M phase cell cycle arrest through DNA damage-
RT induced phosphorylation.";
RL Cell Cycle 7:2705-2709(2008).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KIF11 AND NEK9, AND
RP MUTAGENESIS OF LYS-74 AND LYS-75.
RX PubMed=19001501; DOI=10.1242/jcs.035360;
RA Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C.,
RA Avruch J., Roig J.;
RT "The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site
RT necessary for mitotic spindle formation.";
RL J. Cell Sci. 121:3912-3921(2008).
RN [14]
RP DOMAIN, ACTIVITY REGULATION, AND MUTAGENESIS OF TYR-108.
RX PubMed=19941817; DOI=10.1016/j.molcel.2009.09.038;
RA Richards M.W., O'Regan L., Mas-Droux C., Blot J.M., Cheung J., Hoelder S.,
RA Fry A.M., Bayliss R.;
RT "An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7 kinase
RT is released through binding of Nek9.";
RL Mol. Cell 36:560-570(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NEK9.
RX PubMed=19414596; DOI=10.1128/mcb.01867-08;
RA O'Regan L., Fry A.M.;
RT "The Nek6 and Nek7 protein kinases are required for robust mitotic spindle
RT formation and cytokinesis.";
RL Mol. Cell. Biol. 29:3975-3990(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP FUNCTION, AND INDUCTION.
RX PubMed=21099361; DOI=10.4161/cc.9.23.14059;
RA Jee H.J., Kim A.J., Song N., Kim H.J., Kim M., Koh H., Yun J.;
RT "Nek6 overexpression antagonizes p53-induced senescence in human cancer
RT cells.";
RL Cell Cycle 9:4703-4710(2010).
RN [18]
RP FUNCTION, INTERACTION WITH ANKRA2; ATF4; ARHGAP33; CDC42; CIR1; NEK9;
RP PRAM1; PTN; PRDX3; RAD26L; RBBP6; RPS7 AND TRIP4, PHOSPHORYLATION AT
RP SER-206, AND AUTOPHOSPHORYLATION.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [19]
RP RETRACTED PAPER.
RX PubMed=20407017; DOI=10.1158/1541-7786.mcr-09-0291;
RA Nassirpour R., Shao L., Flanagan P., Abrams T., Jallal B., Smeal T.,
RA Yin M.J.;
RT "Nek6 mediates human cancer cell transformation and is a potential cancer
RT therapeutic target.";
RL Mol. Cancer Res. 8:717-728(2010).
RN [20]
RP RETRACTION NOTICE OF PUBMED:20407017.
RX PubMed=28250205; DOI=10.1158/1541-7786.mcr-16-0440;
RA Nassirpour R., Shao L., Flanagan P., Abrams T., Jallal B., Smeal T.,
RA Yin M.J.;
RT "Retraction: Nek6 Mediates Human Cancer Cell Transformation and Is a
RT Potential Cancer Therapeutic Target.";
RL Mol. Cancer Res. 15:358-358(2017).
RN [21]
RP REVIEW.
RX PubMed=16280549; DOI=10.1242/jcs.02681;
RA Quarmby L.M., Mahjoub M.R.;
RT "Caught Nek-ing: cilia and centrioles.";
RL J. Cell Sci. 118:5161-5169(2005).
RN [22]
RP REVIEW.
RX PubMed=21200151;
RA Fry A.M.;
RT "A role for Nek6 kinase activity in preventing senescence?";
RL Cell Cycle 10:19-20(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP FUNCTION.
RX PubMed=31409757; DOI=10.1126/scisignal.aaw2939;
RA Adib R., Montgomery J.M., Atherton J., O'Regan L., Richards M.W.,
RA Straatman K.R., Roth D., Straube A., Bayliss R., Moores C.A., Fry A.M.;
RT "Mitotic phosphorylation by NEK6 and NEK7 reduces the microtubule affinity
RT of EML4 to promote chromosome congression.";
RL Sci. Signal. 12:0-0(2019).
CC -!- FUNCTION: Protein kinase which plays an important role in mitotic cell
CC cycle progression (PubMed:14563848). Required for chromosome
CC segregation at metaphase-anaphase transition, robust mitotic spindle
CC formation and cytokinesis (PubMed:19414596). Phosphorylates ATF4, CIR1,
CC PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3
CC (PubMed:12054534, PubMed:20873783). Phosphorylates KIF11 to promote
CC mitotic spindle formation (PubMed:19001501). Involved in G2/M phase
CC cell cycle arrest induced by DNA damage (PubMed:18728393). Inhibition
CC of activity results in apoptosis. May contribute to tumorigenesis by
CC suppressing p53/TP53-induced cancer cell senescence (PubMed:21099361).
CC Phosphorylates EML4 at 'Ser-144', promoting its dissociation from
CC microtubules during mitosis which is required for efficient chromosome
CC congression (PubMed:31409757). {ECO:0000269|PubMed:12054534,
CC ECO:0000269|PubMed:14563848, ECO:0000269|PubMed:18728393,
CC ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:19414596,
CC ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:21099361,
CC ECO:0000269|PubMed:31409757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:19001501};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:19001501};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Binding to NEK9 stimulates its activity by
CC releasing the autoinhibitory function of Tyr-108.
CC {ECO:0000269|PubMed:19941817}.
CC -!- SUBUNIT: Interacts with STAT3 and RPS6KB1 (By similarity). Interacts
CC with NEK9, predominantly in mitosis. Interacts with KIF11 (via C-
CC terminus). Interacts with APBB1 (via WW domain). Interacts with ANKRA2,
CC ATF4, ARHGAP33, CDC42, CIR1, PRAM1, PTN, PRDX3, PIN1, RAD26L, RBBP6,
CC RPS7 and TRIP4. {ECO:0000250, ECO:0000269|PubMed:16476580,
CC ECO:0000269|PubMed:17512906, ECO:0000269|PubMed:19001501,
CC ECO:0000269|PubMed:19414596, ECO:0000269|PubMed:20873783}.
CC -!- INTERACTION:
CC Q9HC98; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-740364, EBI-742664;
CC Q9HC98; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-740364, EBI-8638439;
CC Q9HC98; Q13422: IKZF1; NbExp=3; IntAct=EBI-740364, EBI-745305;
CC Q9HC98; Q9UKT9: IKZF3; NbExp=5; IntAct=EBI-740364, EBI-747204;
CC Q9HC98; Q0VD86: INCA1; NbExp=4; IntAct=EBI-740364, EBI-6509505;
CC Q9HC98; Q15323: KRT31; NbExp=3; IntAct=EBI-740364, EBI-948001;
CC Q9HC98; Q6A162: KRT40; NbExp=3; IntAct=EBI-740364, EBI-10171697;
CC Q9HC98; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740364, EBI-739832;
CC Q9HC98; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-740364, EBI-741037;
CC Q9HC98; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-740364, EBI-10172876;
CC Q9HC98; Q13526: PIN1; NbExp=3; IntAct=EBI-740364, EBI-714158;
CC Q9HC98; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-740364, EBI-10172380;
CC Q9HC98; P15884: TCF4; NbExp=4; IntAct=EBI-740364, EBI-533224;
CC Q9HC98; Q08117: TLE5; NbExp=3; IntAct=EBI-740364, EBI-717810;
CC Q9HC98; Q07912: TNK2; NbExp=3; IntAct=EBI-740364, EBI-603457;
CC Q9HC98; P36406: TRIM23; NbExp=4; IntAct=EBI-740364, EBI-740098;
CC Q9HC98; P14373: TRIM27; NbExp=3; IntAct=EBI-740364, EBI-719493;
CC Q9HC98; P98170: XIAP; NbExp=4; IntAct=EBI-740364, EBI-517127;
CC Q9HC98-4; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-11750983, EBI-10181188;
CC Q9HC98-4; O14503: BHLHE40; NbExp=3; IntAct=EBI-11750983, EBI-711810;
CC Q9HC98-4; P27797: CALR; NbExp=3; IntAct=EBI-11750983, EBI-1049597;
CC Q9HC98-4; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-11750983, EBI-11524851;
CC Q9HC98-4; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-11750983, EBI-744556;
CC Q9HC98-4; P12830: CDH1; NbExp=3; IntAct=EBI-11750983, EBI-727477;
CC Q9HC98-4; Q15078: CDK5R1; NbExp=3; IntAct=EBI-11750983, EBI-746189;
CC Q9HC98-4; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11750983, EBI-742887;
CC Q9HC98-4; P27918: CFP; NbExp=3; IntAct=EBI-11750983, EBI-9038570;
CC Q9HC98-4; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-11750983, EBI-3866319;
CC Q9HC98-4; P56545-3: CTBP2; NbExp=3; IntAct=EBI-11750983, EBI-10171902;
CC Q9HC98-4; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11750983, EBI-742054;
CC Q9HC98-4; P17661: DES; NbExp=3; IntAct=EBI-11750983, EBI-1055572;
CC Q9HC98-4; P36957: DLST; NbExp=3; IntAct=EBI-11750983, EBI-351007;
CC Q9HC98-4; Q9BQC3: DPH2; NbExp=3; IntAct=EBI-11750983, EBI-10237931;
CC Q9HC98-4; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-11750983, EBI-2349927;
CC Q9HC98-4; Q7Z4H9: FAM220A; NbExp=3; IntAct=EBI-11750983, EBI-12871772;
CC Q9HC98-4; Q5TD97: FHL5; NbExp=3; IntAct=EBI-11750983, EBI-750641;
CC Q9HC98-4; Q9UPW0: FOXJ3; NbExp=3; IntAct=EBI-11750983, EBI-523002;
CC Q9HC98-4; P14136: GFAP; NbExp=5; IntAct=EBI-11750983, EBI-744302;
CC Q9HC98-4; O75420: GIGYF1; NbExp=3; IntAct=EBI-11750983, EBI-947774;
CC Q9HC98-4; Q8NEA6-2: GLIS3; NbExp=3; IntAct=EBI-11750983, EBI-12232117;
CC Q9HC98-4; Q8N9W4-2: GOLGA6L2; NbExp=3; IntAct=EBI-11750983, EBI-10268729;
CC Q9HC98-4; Q9Y3R0-3: GRIP1; NbExp=3; IntAct=EBI-11750983, EBI-12193965;
CC Q9HC98-4; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-11750983, EBI-10961706;
CC Q9HC98-4; P49639: HOXA1; NbExp=3; IntAct=EBI-11750983, EBI-740785;
CC Q9HC98-4; P17509: HOXB6; NbExp=3; IntAct=EBI-11750983, EBI-741308;
CC Q9HC98-4; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-11750983, EBI-742664;
CC Q9HC98-4; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-11750983, EBI-8638439;
CC Q9HC98-4; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-11750983, EBI-747204;
CC Q9HC98-4; Q0VD86: INCA1; NbExp=3; IntAct=EBI-11750983, EBI-6509505;
CC Q9HC98-4; Q9H079: KATNBL1; NbExp=5; IntAct=EBI-11750983, EBI-715394;
CC Q9HC98-4; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-11750983, EBI-3437878;
CC Q9HC98-4; Q15323: KRT31; NbExp=3; IntAct=EBI-11750983, EBI-948001;
CC Q9HC98-4; O76011: KRT34; NbExp=3; IntAct=EBI-11750983, EBI-1047093;
CC Q9HC98-4; Q6A162: KRT40; NbExp=3; IntAct=EBI-11750983, EBI-10171697;
CC Q9HC98-4; O95678: KRT75; NbExp=3; IntAct=EBI-11750983, EBI-2949715;
CC Q9HC98-4; P05787: KRT8; NbExp=3; IntAct=EBI-11750983, EBI-297852;
CC Q9HC98-4; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11750983, EBI-10171774;
CC Q9HC98-4; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-11750983, EBI-10241252;
CC Q9HC98-4; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-11750983, EBI-1216080;
CC Q9HC98-4; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-11750983, EBI-741037;
CC Q9HC98-4; Q8WWY6: MBD3L1; NbExp=5; IntAct=EBI-11750983, EBI-12516603;
CC Q9HC98-4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11750983, EBI-16439278;
CC Q9HC98-4; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-11750983, EBI-10174029;
CC Q9HC98-4; P15173: MYOG; NbExp=3; IntAct=EBI-11750983, EBI-3906629;
CC Q9HC98-4; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-11750983, EBI-5662487;
CC Q9HC98-4; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-11750983, EBI-10172876;
CC Q9HC98-4; P07196: NEFL; NbExp=3; IntAct=EBI-11750983, EBI-475646;
CC Q9HC98-4; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-11750983, EBI-1055945;
CC Q9HC98-4; Q9GZT8: NIF3L1; NbExp=5; IntAct=EBI-11750983, EBI-740897;
CC Q9HC98-4; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-11750983, EBI-2949792;
CC Q9HC98-4; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-11750983, EBI-10302990;
CC Q9HC98-4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-11750983, EBI-79165;
CC Q9HC98-4; Q6IQ23-2: PLEKHA7; NbExp=3; IntAct=EBI-11750983, EBI-12069346;
CC Q9HC98-4; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-11750983, EBI-710402;
CC Q9HC98-4; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-11750983, EBI-11320284;
CC Q9HC98-4; Q16825: PTPN21; NbExp=3; IntAct=EBI-11750983, EBI-2860264;
CC Q9HC98-4; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-11750983, EBI-1210429;
CC Q9HC98-4; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-11750983, EBI-10182375;
CC Q9HC98-4; P51812: RPS6KA3; NbExp=3; IntAct=EBI-11750983, EBI-1046616;
CC Q9HC98-4; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-11750983, EBI-3957636;
CC Q9HC98-4; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-11750983, EBI-2130111;
CC Q9HC98-4; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-11750983, EBI-12275818;
CC Q9HC98-4; O60504: SORBS3; NbExp=3; IntAct=EBI-11750983, EBI-741237;
CC Q9HC98-4; O43610: SPRY3; NbExp=3; IntAct=EBI-11750983, EBI-12290641;
CC Q9HC98-4; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-11750983, EBI-745958;
CC Q9HC98-4; Q99081-3: TCF12; NbExp=3; IntAct=EBI-11750983, EBI-11952764;
CC Q9HC98-4; P15884-3: TCF4; NbExp=3; IntAct=EBI-11750983, EBI-13636688;
CC Q9HC98-4; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-11750983, EBI-11139477;
CC Q9HC98-4; Q8NA69: TEX45; NbExp=3; IntAct=EBI-11750983, EBI-12021638;
CC Q9HC98-4; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11750983, EBI-1105213;
CC Q9HC98-4; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11750983, EBI-11741437;
CC Q9HC98-4; Q12933: TRAF2; NbExp=3; IntAct=EBI-11750983, EBI-355744;
CC Q9HC98-4; P14373: TRIM27; NbExp=3; IntAct=EBI-11750983, EBI-719493;
CC Q9HC98-4; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-11750983, EBI-2130429;
CC Q9HC98-4; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-11750983, EBI-11524408;
CC Q9HC98-4; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-11750983, EBI-14104088;
CC Q9HC98-4; Q8N3Z6: ZCCHC7; NbExp=3; IntAct=EBI-11750983, EBI-7265024;
CC Q9HC98-4; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-11750983, EBI-11419867;
CC Q9HC98-4; P17028: ZNF24; NbExp=3; IntAct=EBI-11750983, EBI-707773;
CC Q9HC98-4; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-11750983, EBI-10252492;
CC Q9HC98-4; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-11750983, EBI-11962468;
CC Q9HC98-4; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-11750983, EBI-6427977;
CC Q9HC98-4; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-11750983, EBI-4395732;
CC Q9HC98-4; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-11750983, EBI-10251462;
CC Q9HC98-4; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-11750983, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus speckle. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome. Cytoplasm,
CC cytoskeleton, spindle pole. Note=Colocalizes with APBB1 at the nuclear
CC speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with ATF4,
CC CIR1, ARHGAP33, ANKRA2, CDC42, NEK9, RAD26L, RBBP6, RPS7, TRIP4, RELB
CC and PHF1 in the centrosome. Localizes to spindle microtubules in
CC metaphase and anaphase and to the midbody during cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HC98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HC98-2; Sequence=VSP_041798;
CC Name=3;
CC IsoId=Q9HC98-3; Sequence=VSP_041799;
CC Name=4;
CC IsoId=Q9HC98-4; Sequence=VSP_041800;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart and
CC skeletal muscle. {ECO:0000269|PubMed:12054534}.
CC -!- INDUCTION: Up-regulated during the M phase of cell cycle progression.
CC Down-regulated in both replicative and premature senescence of cancer
CC cells. {ECO:0000269|PubMed:14563848, ECO:0000269|PubMed:21099361}.
CC -!- DOMAIN: Displays an autoinhibited conformation: Tyr-108 side chain
CC points into the active site, interacts with the activation loop, and
CC blocks the alphaC helix. The autoinhibitory conformation is released
CC upon binding with NEK9. {ECO:0000269|PubMed:19941817}.
CC -!- PTM: Autophosphorylated. Phosphorylation at Ser-206 is required for its
CC activation. Phosphorylated upon IR or UV-induced DNA damage.
CC Phosphorylated by CHEK1 and CHEK2. Interaction with APBB1 down-
CC regulates phosphorylation at Thr-210. {ECO:0000269|PubMed:12840024,
CC ECO:0000269|PubMed:17512906, ECO:0000269|PubMed:18728393,
CC ECO:0000269|PubMed:20873783}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
CC -!- CAUTION: A paper showing a role in tumorigenesis has been retracted due
CC to panel duplication in several figures. {ECO:0000269|PubMed:20407017,
CC ECO:0000305|PubMed:28250205}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13417.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAH00101.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH04174.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH04209.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA85045.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF087909; AAG13417.1; ALT_SEQ; mRNA.
DR EMBL; AB026289; BAA85045.1; ALT_INIT; mRNA.
DR EMBL; AK294614; BAH11825.1; -; mRNA.
DR EMBL; AK313071; BAG35899.1; -; mRNA.
DR EMBL; AL162724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87579.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87581.1; -; Genomic_DNA.
DR EMBL; BC000101; AAH00101.2; ALT_INIT; mRNA.
DR EMBL; BC004174; AAH04174.2; ALT_INIT; mRNA.
DR EMBL; BC004209; AAH04209.2; ALT_INIT; mRNA.
DR EMBL; BC012761; AAH12761.1; -; mRNA.
DR EMBL; CR457091; CAG33372.1; -; mRNA.
DR EMBL; CR542222; CAG47018.1; -; mRNA.
DR CCDS; CCDS48015.1; -. [Q9HC98-2]
DR CCDS; CCDS55338.1; -. [Q9HC98-3]
DR CCDS; CCDS55339.1; -. [Q9HC98-4]
DR CCDS; CCDS6854.1; -. [Q9HC98-1]
DR PIR; JC7838; JC7838.
DR RefSeq; NP_001138473.1; NM_001145001.2. [Q9HC98-2]
DR RefSeq; NP_001159639.1; NM_001166167.1. [Q9HC98-3]
DR RefSeq; NP_001159640.1; NM_001166168.1. [Q9HC98-1]
DR RefSeq; NP_001159641.1; NM_001166169.1. [Q9HC98-4]
DR RefSeq; NP_001159642.1; NM_001166170.1. [Q9HC98-1]
DR RefSeq; NP_001159643.1; NM_001166171.1. [Q9HC98-2]
DR RefSeq; NP_055212.2; NM_014397.5. [Q9HC98-1]
DR RefSeq; XP_005251721.1; XM_005251664.1. [Q9HC98-1]
DR RefSeq; XP_006716999.1; XM_006716936.2. [Q9HC98-1]
DR RefSeq; XP_016869706.1; XM_017014217.1. [Q9HC98-2]
DR AlphaFoldDB; Q9HC98; -.
DR SMR; Q9HC98; -.
DR BioGRID; 116000; 151.
DR IntAct; Q9HC98; 112.
DR MINT; Q9HC98; -.
DR STRING; 9606.ENSP00000362702; -.
DR BindingDB; Q9HC98; -.
DR ChEMBL; CHEMBL4309; -.
DR DrugCentral; Q9HC98; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR iPTMnet; Q9HC98; -.
DR PhosphoSitePlus; Q9HC98; -.
DR BioMuta; NEK6; -.
DR DMDM; 37537993; -.
DR EPD; Q9HC98; -.
DR jPOST; Q9HC98; -.
DR MassIVE; Q9HC98; -.
DR MaxQB; Q9HC98; -.
DR PaxDb; Q9HC98; -.
DR PeptideAtlas; Q9HC98; -.
DR PRIDE; Q9HC98; -.
DR ProteomicsDB; 81659; -. [Q9HC98-1]
DR ProteomicsDB; 81660; -. [Q9HC98-2]
DR ProteomicsDB; 81661; -. [Q9HC98-3]
DR ProteomicsDB; 81662; -. [Q9HC98-4]
DR Antibodypedia; 30447; 311 antibodies from 32 providers.
DR DNASU; 10783; -.
DR Ensembl; ENST00000320246.10; ENSP00000319734.5; ENSG00000119408.17. [Q9HC98-1]
DR Ensembl; ENST00000373600.7; ENSP00000362702.3; ENSG00000119408.17. [Q9HC98-2]
DR Ensembl; ENST00000373603.5; ENSP00000362705.1; ENSG00000119408.17. [Q9HC98-1]
DR Ensembl; ENST00000394199.6; ENSP00000377749.2; ENSG00000119408.17. [Q9HC98-2]
DR Ensembl; ENST00000539416.5; ENSP00000439651.1; ENSG00000119408.17. [Q9HC98-4]
DR Ensembl; ENST00000540326.5; ENSP00000441469.1; ENSG00000119408.17. [Q9HC98-3]
DR Ensembl; ENST00000545174.5; ENSP00000442636.1; ENSG00000119408.17. [Q9HC98-1]
DR Ensembl; ENST00000546191.5; ENSP00000441426.1; ENSG00000119408.17. [Q9HC98-1]
DR GeneID; 10783; -.
DR KEGG; hsa:10783; -.
DR MANE-Select; ENST00000320246.10; ENSP00000319734.5; NM_014397.6; NP_055212.2.
DR UCSC; uc004bof.4; human. [Q9HC98-1]
DR CTD; 10783; -.
DR DisGeNET; 10783; -.
DR GeneCards; NEK6; -.
DR HGNC; HGNC:7749; NEK6.
DR HPA; ENSG00000119408; Low tissue specificity.
DR MIM; 604884; gene.
DR neXtProt; NX_Q9HC98; -.
DR OpenTargets; ENSG00000119408; -.
DR PharmGKB; PA31550; -.
DR VEuPathDB; HostDB:ENSG00000119408; -.
DR eggNOG; KOG0591; Eukaryota.
DR GeneTree; ENSGT00940000159990; -.
DR InParanoid; Q9HC98; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; Q9HC98; -.
DR TreeFam; TF101021; -.
DR PathwayCommons; Q9HC98; -.
DR Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q9HC98; -.
DR SIGNOR; Q9HC98; -.
DR BioGRID-ORCS; 10783; 22 hits in 1115 CRISPR screens.
DR ChiTaRS; NEK6; human.
DR GeneWiki; NEK6; -.
DR GenomeRNAi; 10783; -.
DR Pharos; Q9HC98; Tchem.
DR PRO; PR:Q9HC98; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9HC98; protein.
DR Bgee; ENSG00000119408; Expressed in sural nerve and 154 other tissues.
DR ExpressionAtlas; Q9HC98; baseline and differential.
DR Genevisible; Q9HC98; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
DR GO; GO:0007077; P:mitotic nuclear membrane disassembly; TAS:Reactome.
DR GO; GO:0007052; P:mitotic spindle organization; TAS:Reactome.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:2000772; P:regulation of cellular senescence; TAS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; TAS:UniProtKB.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IDA:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; TAS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; ATP-binding; Cell cycle; Cell division;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
KW Metal-binding; Microtubule; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..313
FT /note="Serine/threonine-protein kinase Nek6"
FT /id="PRO_0000086427"
FT DOMAIN 45..310
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..44
FT /note="Interaction with ARHGAP33, ANKRA2, CDC42, PRDX3,
FT RAD26L, RBBP6, RPS7 and TRIP4"
FT /evidence="ECO:0000269|PubMed:20873783"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..270
FT /note="Interaction with APBB1"
FT /evidence="ECO:0000269|PubMed:17512906"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 51..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 108
FT /note="Autoinhibitory"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12840024"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12840024"
FT MOD_RES 206
FT /note="Phosphoserine; by NEK9"
FT /evidence="ECO:0000269|PubMed:12840024,
FT ECO:0000269|PubMed:20873783, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17512906"
FT VAR_SEQ 1
FT /note="M -> MPRREVCWEAAHFRQEEQSLPRPRVRALVRLACRM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041798"
FT VAR_SEQ 1
FT /note="M -> MGRRRPAPFRALVRLACRM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041799"
FT VAR_SEQ 1
FT /note="M -> MEATGWDSRCSPGTQVRALVRLACRM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041800"
FT MUTAGEN 74
FT /note="K->M: Loss of autophosphorylation and of kinase
FT activity and induction of apoptosis; when associated with
FT M-75."
FT /evidence="ECO:0000269|PubMed:14563848,
FT ECO:0000269|PubMed:19001501"
FT MUTAGEN 75
FT /note="K->M: Loss of autophosphorylation and of kinase
FT activity and induction of apoptosis; when associated with
FT M-74."
FT /evidence="ECO:0000269|PubMed:14563848,
FT ECO:0000269|PubMed:19001501"
FT MUTAGEN 108
FT /note="Y->A: Increase in catalytic activity."
FT /evidence="ECO:0000269|PubMed:19941817"
FT CONFLICT 88
FT /note="Q -> W (in Ref. 7; CAG33372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35714 MW; B898DC57407A8C16 CRC64;
MAGQPGHMPH GGSSNNLCHT LGPVHPPDPQ RHPNTLSFRC SLADFQIEKK IGRGQFSEVY
KATCLLDRKT VALKKVQIFE MMDAKARQDC VKEIGLLKQL NHPNIIKYLD SFIEDNELNI
VLELADAGDL SQMIKYFKKQ KRLIPERTVW KYFVQLCSAV EHMHSRRVMH RDIKPANVFI
TATGVVKLGD LGLGRFFSSE TTAAHSLVGT PYYMSPERIH ENGYNFKSDI WSLGCLLYEM
AALQSPFYGD KMNLFSLCQK IEQCDYPPLP GEHYSEKLRE LVSMCICPDP HQRPDIGYVH
QVAKQMHIWM SST
